1.O-GlcNAc transferase regulates centriole behavior and intraflagellar transport to promote ciliogenesis.
Fan YU ; Te LI ; Yanchao SUI ; Qingxia CHEN ; Song YANG ; Jia YANG ; Renjie HONG ; Dengwen LI ; Xiumin YAN ; Wei ZHAO ; Xueliang ZHU ; Jun ZHOU
Protein & Cell 2020;11(11):852-857
2.Potential coordination role between O-GlcNAcylation and epigenetics.
Donglu WU ; Yong CAI ; Jingji JIN
Protein & Cell 2017;8(10):713-723
Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GlcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GlcNAcylation as 'protein code' or 'histone code' may provide recognition platforms or executive instructions for subsequent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GlcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O-GlcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GlcNAcylation with epigenetic changes in intracellular biological processes.
Acetylglucosamine
;
metabolism
;
Animals
;
Epigenesis, Genetic
;
Glycoside Hydrolases
;
metabolism
;
Humans
;
N-Acetylglucosaminyltransferases
;
metabolism
;
Neoplasms
;
genetics
;
metabolism
;
Protein Processing, Post-Translational
3.Effects of Xixin decoction on enzymes related to O-GlcNAc glycosylation of tau proteins in the brain of rats with sporadic Alzheimer's disease.
Yongchang DIWU ; Jinzhou TIAN ; Jing SHI
Journal of Southern Medical University 2013;33(10):1442-1447
OBJECTIVETo study the effects of Xixin decoction (XXD) on O-GlcNAc transferase (OGT) and O-GlcNAc glycosidase in O-GlcNAc glycosylation of tau proteins in the brain of rats with sporadic Alzheimer's disease (SAD) and explore the possible mechanism.
METHODSMale SD rats were randomly divided into sham-operated group, model group, donepezil group, and low-, moderate-, and high-dose XXD groups. After treatment and behavioral test, the rats were sacrificed for detecting the expressions of OGT and O-GlcNAc glycosidase in the brain using immunohistochemistry and Western blotting.
RESULTSXXD significantly enhanced the expressions of OGT in the hippocampus of SAD rats and lowered the expression of O-GlcNAc glycosidase (P<0.05 or 0.01). OGT and O-GlcNAc glycosidase expressions showed no significant differences between the model group and donepezil group (P>0.05).
CONCLUSIONXXD can regulate the expression of OGT and O-GlcNAc glycosidase to enhance O-GlcNAc glycosylation of tau proteins in the hippocampus of SAD rats.
Acetylglucosaminidase ; metabolism ; Alzheimer Disease ; chemically induced ; enzymology ; metabolism ; Animals ; Dose-Response Relationship, Drug ; Drugs, Chinese Herbal ; administration & dosage ; pharmacology ; Glycosylation ; Hippocampus ; enzymology ; metabolism ; Male ; N-Acetylglucosaminyltransferases ; metabolism ; Random Allocation ; Rats ; Rats, Sprague-Dawley ; Streptozocin ; tau Proteins ; metabolism
4.Biosynthesis of chitooligosaccharides by recombinant Escherichia coli.
Da-Wei ZHANG ; Jie CHU ; Yong-Ren HAO ; Ming-Hua LI ; Peng WANG
Chinese Journal of Biotechnology 2007;23(3):525-529
Acetyl-N-glucosaminyltransferase gene (nodC) was successfully cloned to Escherichia coli from Mesorhizobium loti. The recombinant E. coli harboring nodC gene was able to synthesize chitooligosaccharides (COs) in MMYNG medium. In optimized condition, a yield of 526 mg/L was obtained after 26 h cultivation in 10 L bioreactor. COs concentration reached up to 4.5% of the cell dry weight. The COs products were purified by charcoal adsorption and Bio-gel P4 chromatography, penta-N-acetylchitopentaose (m/z, 1034[M + H]+) and tetra-N-acetylchitopentaose (m/z, 831 [M + H]+) were identified as the dominating COs product using the method of liquid chromatography-electrospray ionization mass spectrometry (LC-ESI-MS).
Bacterial Proteins
;
genetics
;
metabolism
;
Chitosan
;
isolation & purification
;
metabolism
;
Chromatography, Gel
;
Chromatography, High Pressure Liquid
;
Escherichia coli
;
genetics
;
metabolism
;
N-Acetylglucosaminyltransferases
;
genetics
;
metabolism
;
Oligosaccharides
;
biosynthesis
;
isolation & purification
;
Recombinant Proteins
;
metabolism
;
Spectrometry, Mass, Electrospray Ionization
5.Acute UV Irradiation Increases Heparan Sulfate Proteoglycan Levels in Human Skin.
Ji Yong JUNG ; Jang Hee OH ; Yeon Kyung KIM ; Mi Hee SHIN ; Dayae LEE ; Jin Ho CHUNG
Journal of Korean Medical Science 2012;27(3):300-306
Glycosaminoglycans are important structural components in the skin and exist as various proteoglycan forms, except hyaluronic acid. Heparan sulfate (HS), one of the glycosaminoglycans, is composed of repeated disaccharide units, which are glucuronic acids linked to an N-acetyl-glucosamine or its sulfated forms. To investigate acute ultraviolet (UV)-induced changes of HS and HS proteoglycans (HSPGs), changes in levels of HS and several HSPGs in male human buttock skin were examined by immunohistochemistry and real-time quantitative polymerase chain reaction (qPCR) after 2 minimal erythema doses (MED) of UV irradiation (each n = 4-7). HS staining revealed that 2 MED of UV irradiation increased its expression, and staining for perlecan, syndecan-1, syndecan-4, CD44v3, and CD44 showed that UV irradiation increased their protein levels. However, analysis by real-time qPCR showed that UV irradiation did not change mRNA levels of CD44 and agrin, and decreased perlecan and syndecan-4 mRNA levels, while increased syndecan-1 mRNA level. As HS-synthesizing or -degrading enzymes, exostosin-1 and heparanase mRNA levels were increased, but exostosin-2 was decreased by UV irradiation. UV-induced matrix metalloproteinase-1 expression was confirmed for proper experimental conditions. Acute UV irradiation increases HS and HSPG levels in human skin, but their increase may not be mediated through their transcriptional regulation.
Adult
;
Agrin/genetics
;
Antigens, CD44/genetics
;
Base Sequence
;
DNA Primers/genetics
;
Gene Expression/radiation effects
;
Glucuronidase/genetics
;
Heparan Sulfate Proteoglycans/genetics/*metabolism
;
Heparitin Sulfate/metabolism
;
Humans
;
Male
;
Matrix Metalloproteinase 1/genetics
;
N-Acetylglucosaminyltransferases/genetics
;
RNA, Messenger/genetics/metabolism
;
Skin/*metabolism/*radiation effects
;
Skin Aging/genetics/physiology
;
Syndecan-1/genetics
;
Syndecan-4/genetics
;
Ultraviolet Rays/*adverse effects
;
Young Adult